Preparation and Characterization of Iron-chelating Peptides from Silver Carp Scale Collagen
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Abstract:
Silver carp scale collagen peptides were chelated with ferrous ions, with the chelation rate as an evaluation index. The optimum preparation conditions for the iron-chelating collagen peptides were explored and their molecular weight distribution, amino acid composition, and structure were characterized via single factor experiments and response surface analysis. The optimal preparation conditions for the iron-chelating collagen peptides were as follows: pH, 7.5; peptide-iron mass ratio, 5:1; peptide solution mass fraction, 2.5%; chelating time, 40 min; and chelating temperature, 35 ℃. Under these conditions, the chelation rate of iron was 92.04%. According to the analysis of molecular weight distribution and amino acid composition, after collagen peptide and Fe2+ chelation, the proportion of molecular weight below 1 000 u decreased, with glutamic acid, aspartic acid, alanine, valine, and arginine in the collagen peptides playing important roles in the chelation reaction. Furthermore, the X-ray diffraction patterns showed that iron-chelating peptides from silver carp scale collagen had an amorphous structure, unlike collagen peptide. This study is expected to serve as a reference for the preparation, optimization, and structural characterization of iron-chelating peptides from silver carp collagen.
